ID A0A0K8NYN2_IDESA Unreviewed; 727 AA.
AC A0A0K8NYN2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ISF6_1264 {ECO:0000313|EMBL:GAP35491.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP35491.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP35491.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAP35491.1}.
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DR EMBL; BBYR01000023; GAP35491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8NYN2; -.
DR STRING; 1547922.ISF6_1264; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF50; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GAP35491.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037660};
KW Transferase {ECO:0000313|EMBL:GAP35491.1}.
FT DOMAIN 145..190
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 241..293
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 465..691
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 426..456
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 727 AA; 76658 MW; 6411ECE73180FAA0 CRC64;
MSVASTDSAA TAPAAVPAWL EAVAVPAALW QAGRLGAANE AFARLARREA AALAGCRLDG
LVAAEDLAAL DRALGDAATG AGLPPVVSAR LLTPDGGERP VEIHARPLAR DGRPAAVPGD
APPPVLLTCL DQSDIQHVQT SLFALSGLLG QIVDGAPLAT LVIDAAHRVT HWNAACERLT
GLARREVVGR REAWRAMFTA PRPMLADLIV DGIDAAAAAA RRGGEGEGEA VVASRAVPGG
LALEAWFPQF GPEGAWLYAT AAPLRDAEGR VVGAIETLQD VSRRRRTEQE LQRHRDELED
LVRRRSAELA ATADELAQFI EEAPIGVAWS CEGVLQRANP ALVAMLGERP GGWVGAPLAE
LGLPPDLVAR ARALDPAAAA LHAEAWLRRA DGGEIWVQVD ARAAAGPQAA GLWWMMQDRS
EIRAAHEVLH SRVDELRETN HRLEEAQNQL LQQDKMAMIG QLAAGVAHEI NNPIAFVGAN
LNTLRHYADE LLRRIAGDDA GGPQALAELR EDLPVLLDEC ADGLGRVRKI VQDLKDFSRV
DQADWQEADL NAGLESTLNV LRHELKYKAR VERRLGVLPP VRCLPGQLNQ VFMNLVVNAS
QALGEAGTVT LSSGTEGPWA WVQVDDDGCG MPEAVRRRIF EPFFTTKDVG KGTGLGLSLS
FSIVKKHGGA IQVRSAPGAG SSFRVWVPVG GPGAVAGQAV PAAWQDAPGP GPGPGLAVCA
AAPGPSA
//
